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Combined biochemical and immunocytochemical analyses of citrulline-containing proteins in rat epidermis and hair roots generated by peptidylarginine deiminase reactions
JSID Abstracts/J.
Dermatol. Sci. 8 (1994) 54-88
71
097
100
MDLECULAR CLONING OF A cDNAENCODING A NOVELFAITY ACID-BINDING PKUTEINFKOM KATSKIN
AN EFFECT OF SINGLE APPLICATION OF TOPICAL STEROID ON THE MORPHOLOGIES OF EPfMRMAL LANGERHANSCELLS T. MIYAGI , T. KAMIYAMA , T.KiNJOU and S. NONAKA , Department of
R. WATANABE, A. YAMAMDTO and Y. ITO. Departaent of Dereetology, Niigata University School of Medicine, Niigata 951, Japan
Dermatology,
Faculty
of Medicine,
University
of the Ryukyus,
It is a well known fact that steroid supresses Langerhans This
A novel skin-type fatty acid-binding protein. termed cutaneous(C) FABP, has been purified froa rat skin and a cDNAclone for this protein has been identified. The purified protein had the ability to bind long chain fatty acids like other rat FABPs. The deduced -ino acid sequence of the cDNAclone cmprises residues yielding a qolecular aasa for the palypeptide of 15.1 kDa and exhibits around 50 % identity to nyelin P2 protein. adipacyte FABPand heart FABP. Our results prwwe that C-FABPis a new r&w of the FABPfamily.
Okinawa,
Japan implies that steroid have a negative
antigen-presenting
functions.
effect
cell(LC)
on LC activity
number.
such ss the
Steroids are the agents most commonly
used
for the treatment of the skin diseases. But there is very little studies on the effects of single application of topical steroids on LC. In this study, we investigate steroid effects on morphologic changes of LC. Hartley strain guinea pigs were used for this study. Single application propionate
was applied
to the dorsa
number was observed, but single application suggests
that
singk application
morphofoguzal
sites of the steroid
there
of guinea
is a possibility
charges
compared
that
of 0.05%
pigs.
cbbetasol
No change
in LC
of LC were seen in the with
control
immunosuppression
site. occurs
This by
of the topical steroid.
101 EFFECTS OF PROTEASE INHIBITORS DESMOSOMES Y .Suzuki,
OF STRATUM
AND Ca*+ ON DEGRADATION
OF
CORNEUMSHEETIN VITRO.
COMBINED BIOCHEMICAL AND lMMUNOCYTOCHEMlCAL ANALYSES OF CITRULLINE-CONTAINING PROTEINS IN RAT EPIDERMIS AND HAIR ROOTS GENERATED BY PEPTIDYLARGININE DEIMINASE REACTIONS T. SENSHU and K. AKIYAMA Department of Ceil Chemistry, Tokyo, Japan
O.Moro. J.Nomura, J.Koyama and I.Horii,
Shiseido Research Center, Yokohama, Japan We previouslyreportedthat bothnypsin-likeandchymotrypsin-like wine proleases are involvedin stratumcomeurn(SC) desquamadon.The aim of this work was to elucidatewhetherthesepmtues degradedesmoglein-I@G-l) anddesmocollin(DC) in stratumcomeurn.We examinedthedegradation of DG-I andDC duringincubation in the presenceandabsenceof proceaseinhibitors.Antibodiesraisedagainstbovine
Citrulliw l++,
Tokyo Metropdian
Institute of Gerontology.
is nal +orporated into proteins by ths ordinary biosynthetic @way. dtrulkne residuee have been found by ths arnbm aofd ~afyses of tr&bnsofthehdrmedu2a,lheWemdrodshedhdhak
DG-1 and DC were used in immunoblot analysis of human SC sheet. After 24-h innbation of SC she& in Tris buffer witbout proteaseinhibirors, D&I
and DC weR
degrxkd completely. but in tk. presenceof qrotinin 01 a mixture of leupepdn and chymostatin. Do-1 and DC remained in the SC sheet. These resultsindicate thaf bothproteasesare requiredfor the degradationof DC-I and DC. Ca*+ (2mM)also inhibitedthe degradationof DO-1 and DC. ConsideringlbatCa2+ (2mM) inhibited the activities of the fwo proteases by less than 20%. Cs2+ may regulate desmasomalLgmdationby increasingIIKproteaseresistanceof DG-I andDC.
minated proteins in Ion may be fnvolved i the epidenis.
102 Differentiation-Associated Localization of sprl in Normal Human Skin and Skin Diseases H. Koizumi’, H. Tanaka’- T. Karta.sova*. A. Ohkawara’. and T. Kurokii, ‘Department of Dermatology. Hokkaido University School of Medicine, and *Department of Cancer Cell Research, Institute of MedIcal Science, University of Tokyo Sorl fsmall orolin rich) was orioinaflv Isolated from a human epidermai cDNA library as UV-inducibfe. Thi ex~essfon of this gene is indu&i during epidermal differentiation. The presence and locafization of sprl protein in normal human skin and diseased skin have been demonstrated using ImmunoMot and lmmunohlstochemical staining. A polycfonai antlbody was raised against a synthetic peptfde at the C terminal region of the spri molecule. im&noblot~anaiysls of normal human epidermis revealed that the eokiermis contains a 18 kDa immunoreactive WOtein. in normal skin, the s&g staining was observed in the uppermost i few living ceil layers of epldermls and was obvious in the membrane and the cytoplasm. in psoriatic skin, stalned keratinocytes were distributed in the living ceil layers except basal layer. in squamous ceil carcinoma, the staining was weak In keratotfc cells around horny pearis. In basal cell epithelbma the tumor ceils were not stained. in imthyoeis eprl was barely expressed. in acantholk epkiermk in eczema and my& fungoides sprl was expressed with a slmiiar pattern as that of psoriasis. -r
%-
r
EXPRESSIONPATTERNSOF COf?NIFiiVSPFiR1IN NORMALSKIN. MUCOUS EPITHELIUMAND VARfASLESKIN DISEASES W. FUJIMOTO’, G. NAKANISHI’, J. ARATA’ and A.M.JElTEN2 1 Department of Dermatobgy, Okayama University Medical School, and 2 NIEHS. NIH. ResearchTriingk Park, NC, U.S.A. Comifin is a proline rich protein expressed late in epkfermal differentiation. It acts as substrates for transgfulaminase type I and beoomes integrated into comified call envelope. In this study, expression paftems of oomfffn in normal epidermis, in oral mucws epiihelfum and in hair folfff were analyzed using immunohisfobov with wivobnal anfibody SQ37C lo a unioue carboxy terminal peptide of hu& o&fin, sprl-1 and-were compared with the p&ems of
expression of fnvolucrinand bxicrin. In additbn.135 f3io@es from a wide range of skin diseases wera studied Immunoh~ ffy. In muoous epitheiium. abundant expression of oomifin was datsctsd in upfw sqsrnows osll layers. In hair foffiife, oorniffn expression was fimfted to innerwt layers of outer root sheafh, and uppr pail of inner root slwafh. Comiffn expmsslon was augmented in pwakerafotk fteraUni&on as obmrvad In psorlsclis. pffyrfasis mbm. VBrmoa andwdl~renHPted~uecallcarcinoma.Hbhlevekof~~werealso found in hypergmnubif epidermis as obse& in lichen PknuS, and In degenerative epidermis as observed in neorolyfk migratory eryihema. Our results indfoste (1) that oomhin expreesion fs dosefy Wad wfth hyparpfasfio, squamous-dfffemntlatad epfr&smrfs and qMeflum end (2) that oomifin has an addltfnal functbn in hair follicle ofher fhan oomlffed ceil envebps formation.
Dermatol. Sci. 8 (1994) 54-88
71
097
100
MDLECULAR CLONING OF A cDNAENCODING A NOVELFAITY ACID-BINDING PKUTEINFKOM KATSKIN
AN EFFECT OF SINGLE APPLICATION OF TOPICAL STEROID ON THE MORPHOLOGIES OF EPfMRMAL LANGERHANSCELLS T. MIYAGI , T. KAMIYAMA , T.KiNJOU and S. NONAKA , Department of
R. WATANABE, A. YAMAMDTO and Y. ITO. Departaent of Dereetology, Niigata University School of Medicine, Niigata 951, Japan
Dermatology,
Faculty
of Medicine,
University
of the Ryukyus,
It is a well known fact that steroid supresses Langerhans This
A novel skin-type fatty acid-binding protein. termed cutaneous(C) FABP, has been purified froa rat skin and a cDNAclone for this protein has been identified. The purified protein had the ability to bind long chain fatty acids like other rat FABPs. The deduced -ino acid sequence of the cDNAclone cmprises residues yielding a qolecular aasa for the palypeptide of 15.1 kDa and exhibits around 50 % identity to nyelin P2 protein. adipacyte FABPand heart FABP. Our results prwwe that C-FABPis a new r&w of the FABPfamily.
Okinawa,
Japan implies that steroid have a negative
antigen-presenting
functions.
effect
cell(LC)
on LC activity
number.
such ss the
Steroids are the agents most commonly
used
for the treatment of the skin diseases. But there is very little studies on the effects of single application of topical steroids on LC. In this study, we investigate steroid effects on morphologic changes of LC. Hartley strain guinea pigs were used for this study. Single application propionate
was applied
to the dorsa
number was observed, but single application suggests
that
singk application
morphofoguzal
sites of the steroid
there
of guinea
is a possibility
charges
compared
that
of 0.05%
pigs.
cbbetasol
No change
in LC
of LC were seen in the with
control
immunosuppression
site. occurs
This by
of the topical steroid.
101 EFFECTS OF PROTEASE INHIBITORS DESMOSOMES Y .Suzuki,
OF STRATUM
AND Ca*+ ON DEGRADATION
OF
CORNEUMSHEETIN VITRO.
COMBINED BIOCHEMICAL AND lMMUNOCYTOCHEMlCAL ANALYSES OF CITRULLINE-CONTAINING PROTEINS IN RAT EPIDERMIS AND HAIR ROOTS GENERATED BY PEPTIDYLARGININE DEIMINASE REACTIONS T. SENSHU and K. AKIYAMA Department of Ceil Chemistry, Tokyo, Japan
O.Moro. J.Nomura, J.Koyama and I.Horii,
Shiseido Research Center, Yokohama, Japan We previouslyreportedthat bothnypsin-likeandchymotrypsin-like wine proleases are involvedin stratumcomeurn(SC) desquamadon.The aim of this work was to elucidatewhetherthesepmtues degradedesmoglein-I@G-l) anddesmocollin(DC) in stratumcomeurn.We examinedthedegradation of DG-I andDC duringincubation in the presenceandabsenceof proceaseinhibitors.Antibodiesraisedagainstbovine
Citrulliw l++,
Tokyo Metropdian
Institute of Gerontology.
is nal +orporated into proteins by ths ordinary biosynthetic @way. dtrulkne residuee have been found by ths arnbm aofd ~afyses of tr&bnsofthehdrmedu2a,lheWemdrodshedhdhak
DG-1 and DC were used in immunoblot analysis of human SC sheet. After 24-h innbation of SC she& in Tris buffer witbout proteaseinhibirors, D&I
and DC weR
degrxkd completely. but in tk. presenceof qrotinin 01 a mixture of leupepdn and chymostatin. Do-1 and DC remained in the SC sheet. These resultsindicate thaf bothproteasesare requiredfor the degradationof DC-I and DC. Ca*+ (2mM)also inhibitedthe degradationof DO-1 and DC. ConsideringlbatCa2+ (2mM) inhibited the activities of the fwo proteases by less than 20%. Cs2+ may regulate desmasomalLgmdationby increasingIIKproteaseresistanceof DG-I andDC.
minated proteins in Ion may be fnvolved i the epidenis.
102 Differentiation-Associated Localization of sprl in Normal Human Skin and Skin Diseases H. Koizumi’, H. Tanaka’- T. Karta.sova*. A. Ohkawara’. and T. Kurokii, ‘Department of Dermatology. Hokkaido University School of Medicine, and *Department of Cancer Cell Research, Institute of MedIcal Science, University of Tokyo Sorl fsmall orolin rich) was orioinaflv Isolated from a human epidermai cDNA library as UV-inducibfe. Thi ex~essfon of this gene is indu&i during epidermal differentiation. The presence and locafization of sprl protein in normal human skin and diseased skin have been demonstrated using ImmunoMot and lmmunohlstochemical staining. A polycfonai antlbody was raised against a synthetic peptfde at the C terminal region of the spri molecule. im&noblot~anaiysls of normal human epidermis revealed that the eokiermis contains a 18 kDa immunoreactive WOtein. in normal skin, the s&g staining was observed in the uppermost i few living ceil layers of epldermls and was obvious in the membrane and the cytoplasm. in psoriatic skin, stalned keratinocytes were distributed in the living ceil layers except basal layer. in squamous ceil carcinoma, the staining was weak In keratotfc cells around horny pearis. In basal cell epithelbma the tumor ceils were not stained. in imthyoeis eprl was barely expressed. in acantholk epkiermk in eczema and my& fungoides sprl was expressed with a slmiiar pattern as that of psoriasis. -r
%-
r
EXPRESSIONPATTERNSOF COf?NIFiiVSPFiR1IN NORMALSKIN. MUCOUS EPITHELIUMAND VARfASLESKIN DISEASES W. FUJIMOTO’, G. NAKANISHI’, J. ARATA’ and A.M.JElTEN2 1 Department of Dermatobgy, Okayama University Medical School, and 2 NIEHS. NIH. ResearchTriingk Park, NC, U.S.A. Comifin is a proline rich protein expressed late in epkfermal differentiation. It acts as substrates for transgfulaminase type I and beoomes integrated into comified call envelope. In this study, expression paftems of oomfffn in normal epidermis, in oral mucws epiihelfum and in hair folfff were analyzed using immunohisfobov with wivobnal anfibody SQ37C lo a unioue carboxy terminal peptide of hu& o&fin, sprl-1 and-were compared with the p&ems of
expression of fnvolucrinand bxicrin. In additbn.135 f3io@es from a wide range of skin diseases wera studied Immunoh~ ffy. In muoous epitheiium. abundant expression of oomifin was datsctsd in upfw sqsrnows osll layers. In hair foffiife, oorniffn expression was fimfted to innerwt layers of outer root sheafh, and uppr pail of inner root slwafh. Comiffn expmsslon was augmented in pwakerafotk fteraUni&on as obmrvad In psorlsclis. pffyrfasis mbm. VBrmoa andwdl~renHPted~uecallcarcinoma.Hbhlevekof~~werealso found in hypergmnubif epidermis as obse& in lichen PknuS, and In degenerative epidermis as observed in neorolyfk migratory eryihema. Our results indfoste (1) that oomhin expreesion fs dosefy Wad wfth hyparpfasfio, squamous-dfffemntlatad epfr&smrfs and qMeflum end (2) that oomifin has an addltfnal functbn in hair follicle ofher fhan oomlffed ceil envebps formation.